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Zinc in PDB 4a91: Crystal Structure of the Glutamyl-Queuosine Trnaasp Synthetase From E. Coli Complexed with L-Glutamate

Protein crystallography data

The structure of Crystal Structure of the Glutamyl-Queuosine Trnaasp Synthetase From E. Coli Complexed with L-Glutamate, PDB code: 4a91 was solved by M.Blaise, V.Olieric, C.Sauter, B.Lorber, B.Roy, S.Karmakar, R.Banerjee, H.D.Becker, D.Kern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.35 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 39.100, 115.030, 154.400, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 19.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Glutamyl-Queuosine Trnaasp Synthetase From E. Coli Complexed with L-Glutamate (pdb code 4a91). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Glutamyl-Queuosine Trnaasp Synthetase From E. Coli Complexed with L-Glutamate, PDB code: 4a91:

Zinc binding site 1 out of 1 in 4a91

Go back to Zinc Binding Sites List in 4a91
Zinc binding site 1 out of 1 in the Crystal Structure of the Glutamyl-Queuosine Trnaasp Synthetase From E. Coli Complexed with L-Glutamate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Glutamyl-Queuosine Trnaasp Synthetase From E. Coli Complexed with L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:16.9
occ:1.00
OH A:TYR115 2.1 17.3 1.0
SG A:CYS119 2.4 17.0 1.0
SG A:CYS101 2.4 16.3 1.0
SG A:CYS103 2.4 19.6 1.0
CZ A:TYR115 3.0 16.8 1.0
CE1 A:TYR115 3.2 17.4 1.0
CB A:CYS119 3.3 16.1 1.0
CB A:CYS103 3.3 20.3 1.0
CB A:CYS101 3.4 13.5 1.0
N A:CYS103 3.7 18.6 1.0
N A:CYS119 3.7 17.3 1.0
CA A:CYS101 3.8 15.9 1.0
N A:THR102 3.9 18.6 1.0
CA A:CYS103 4.1 21.2 1.0
CB A:HIS118 4.1 18.6 1.0
CA A:CYS119 4.1 16.1 1.0
ND1 A:HIS118 4.1 26.4 1.0
C A:CYS101 4.2 17.4 1.0
CE2 A:TYR115 4.2 19.0 1.0
O A:HOH685 4.4 36.7 1.0
CD1 A:TYR115 4.6 14.0 1.0
C A:HIS118 4.6 17.4 1.0
CG A:HIS118 4.6 23.1 1.0
C A:THR102 4.7 23.3 1.0
CA A:HIS118 4.7 17.8 1.0
NE A:ARG132 4.8 14.3 1.0
CA A:THR102 4.9 19.2 1.0
N A:HIS118 4.9 16.5 1.0

Reference:

M.Blaise, V.Olieric, C.Sauter, B.Lorber, B.Roy, S.Karmakar, R.Banerjee, H.D.Becker, D.Kern. Crystal Structure of Glutamyl-Queuosine Trnaasp Synthetase Complexed with L-Glutamate: Structural Elements Mediating Trna-Independent Activation of Glutamate and Glutamylation of Trnaasp Anticodon. J.Mol.Biol. V. 381 1224 2008.
ISSN: ISSN 0022-2836
PubMed: 18602926
DOI: 10.1016/J.JMB.2008.06.053
Page generated: Wed Dec 16 05:02:36 2020

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